Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA
|Corresponding Author||Sui，Sen Fang; Dong，Yuhui; Li，Yanhua|
|Joint first author||Yang，Xiaoyun|
PldA, a phospholipase D (PLD) effector, catalyzes hydrolysis of the phosphodiester bonds of glycerophospholipids-the main component of cell membranes-and assists the invasion of the opportunistic pathogen Pseudomonas aeruginosa. As a cognate immunity protein, PA3488 can inhibit the activity of PldA to avoid self-toxicity. However, the precise inhibitory mechanism remains elusive. We determine the crystal structures of full-length and truncated PldA and the cryogenic electron microscopy structure of the PldA-PA3488 complex. Structural analysis reveals that there are different intermediates of PldA between the "open" and "closed" states of the catalytic pocket, accompanied by significant conformational changes in the "lid" region and the peripheral helical domain. Through structure-based mutational analysis, we identify the key residues responsible for the enzymatic activity of PldA. Together, these data provide an insight into the molecular mechanisms of PldA invasion and its neutralization by PA3488, aiding future design of PLD-targeted inhibitors and drugs.
NI Journal Papers
First ; Corresponding
Beijing Municipal Science and Technology Commission[Z191100007219007]
|WOS Research Area|
Science & Technology - Other Topics
|WOS Accession No|
Cited Times [WOS]:1
|Document Type||Journal Article|
|Department||Department of Biology|
1.Department of Biology,Southern University of Science and Technology,Guangdong Province,Shenzhen,518055,China
2.Multidiscipline Research Center,Institute of High Energy Physics,Chinese Academy of Sciences,China
3.State Key Laboratory of Membrane Biology,Beijing Advanced Innovation Center for Structural Biology,Beijing Frontier Research Center for Biological Structure,Tsinghua-Peking Center for Life Sciences,School of Life Sciences,Tsinghua University,100084,China
|First Author Affilication||Department of Biology; School of Life Sciences|
|Corresponding Author Affilication||Department of Biology; School of Life Sciences|
|First Author's First Affilication||Department of Biology; School of Life Sciences|
Yang，Xiaoyun,Li，Zongqiang,Zhao，Liang,et al. Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA[J]. Nature communications,2022,13(1).
Yang，Xiaoyun.,Li，Zongqiang.,Zhao，Liang.,She，Zhun.,Gao，Zengqiang.,...&Li，Yanhua.(2022).Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA.Nature communications,13(1).
Yang，Xiaoyun,et al."Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA".Nature communications 13.1(2022).
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